ID A0A0Q5ZB84_9BURK Unreviewed; 336 AA.
AC A0A0Q5ZB84;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KQT11273.1};
GN ORFNames=ASG30_05165 {ECO:0000313|EMBL:KQT11273.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT11273.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT11273.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT11273.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT11273.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT11273.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQT11273.1}.
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DR EMBL; LMQL01000009; KQT11273.1; -; Genomic_DNA.
DR RefSeq; WP_055895142.1; NZ_LMQL01000009.1.
DR AlphaFoldDB; A0A0Q5ZB84; -.
DR STRING; 1736365.ASG30_05165; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT DOMAIN 27..191
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 336 AA; 36183 MW; 5D596A31B7CC82C5 CRC64;
MNTVTADKKP RLTTSAMIAS IASEGQRVKA APFGKALVEY AASRPHVVGL TADLAKYTDL
HLFAQAYPER FFQMGMAEQL LMGAAGGLAK EGLVPFATTY AVFGTRRAYD FIHQVIAEEN
LNVKICCALP GLTTGYGPSH QATEDLAMMR AVPGLTVVDP CDALDIEQAV PQIAEHKGPV
YMRLLRGSVP LVLDEVEGYR FELGKAKMLR EGADVLVISS GILTMRALEV AKDLAADNIG
VAVLHCPTIK PLDEAAIVEA VRYQHRLVVV AENHSVVGGL GEAVASALLR NRVQPARFEL
AGLPDAFLDA GALPTLHERY GISREALTSR IKRWLG
//
